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Q47QS9 (HISX_THEFY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:Tfu_1150
OrganismThermobifida fusca (strain YX) [Complete proteome] [HAMAP]
Taxonomic identifier269800 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135868

Sites

Active site3301Proton acceptor By similarity
Active site3311Proton acceptor By similarity
Metal binding2611Zinc By similarity
Metal binding2641Zinc By similarity
Metal binding3641Zinc By similarity
Metal binding4231Zinc By similarity
Binding site1291NAD By similarity
Binding site1931NAD By similarity
Binding site2161NAD By similarity
Binding site2391Substrate By similarity
Binding site2611Substrate By similarity
Binding site2641Substrate By similarity
Binding site3311Substrate By similarity
Binding site3641Substrate By similarity
Binding site4181Substrate By similarity
Binding site4231Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47QS9 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: C6657EAC246CA868

FASTA43845,811
        10         20         30         40         50         60 
MRSVISRIDL RGNPADPRAS LPRAEIDVAS AVEKVRPICE DVRHRGVEAL IELGERFDGV 

        70         80         90        100        110        120 
RPAHIRVPAD ALETALAGLD RTVRAALEEA IRRARIVHRD QRRTDTTTRV VPGGTVTERW 

       130        140        150        160        170        180 
VPVDRVGLYV PGGRAVYPSS VVMNVVPAQE AGVPSLAVAS PPQAEFGGLP HPTILAACAL 

       190        200        210        220        230        240 
LGVDEVYAVG GAQAIAMFAY GAGECAPVSM VTGPGNIWVA AAKRLLKGII GIDSEAGPTE 

       250        260        270        280        290        300 
IAILADDTAN PAYVAADLIS QAEHDVVAAS VLVTPSTALA DRVEAELARQ VPAAKHRERI 

       310        320        330        340        350        360 
TQALGGPQSG IVLVDDIDHG LDVVNAYAPE HLEVMTADAQ SVAARVRNAG AIFIGDHSPV 

       370        380        390        400        410        420 
SLGDYCAGSN HVLPTGGVAV HSSGLSVQSF LRGIHVVEYD RAALAEVAHH VVALAEAEDL 

       430 
PAHGAAVTAR IPREEQQA 

« Hide

References

[1]"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX."
Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N.
J. Bacteriol. 189:2477-2486(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000088 Genomic DNA. Translation: AAZ55188.1.
RefSeqYP_289211.1. NC_007333.1.

3D structure databases

ProteinModelPortalQ47QS9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269800.Tfu_1150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ55188; AAZ55188; Tfu_1150.
GeneID3581196.
KEGGtfu:Tfu_1150.
PATRIC23902804. VBITheFus33945_1202.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAQKSLHAV.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycTFUS269800:GI42-1168-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_THEFY
AccessionPrimary (citable) accession number: Q47QS9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways